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Protein

Glutathione biosynthesis bifunctional protein GshAB

Gene

gshAB

Organism
Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Synthesizes glutathione from L-glutamate and L-cysteine via gamma-L-glutamyl-L-cysteine.

Catalytic activityi

ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine.UniRule annotation
ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione.UniRule annotation

Cofactori

Mg2+By similarity, Mn2+By similarityNote: Binds 2 magnesium or manganese ions per subunit.By similarity

Enzyme regulationi

Inhibited by L-buthionine-S-sulfoximine (L-S-BSO).

Kineticsi

  1. KM=22 mM for L-glutamate
  2. KM=156 µM for L-cysteine
  3. KM=8.2 mM for alpha-L-aminobutyrate
  4. KM=64 µM for ATP (in the reaction with gamma-GCS)
  5. KM=5.9 mM for gamma-L-glutamyl-L-cysteine
  6. KM=11.5 mM for gamma-L-glutamyl-L-alpha-aminobutyrate
  7. KM=6.3 mM for glycine
  8. KM=420 µM for ATP (in the reaction with GS)

    Pathwayi: glutathione biosynthesis

    This protein is involved in step 1 and 2 of the subpathway that synthesizes glutathione from L-cysteine and L-glutamate.UniRule annotation
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. Glutathione biosynthesis bifunctional protein GshAB (gshAB)
    2. Glutathione biosynthesis bifunctional protein GshAB (gshAB)
    This subpathway is part of the pathway glutathione biosynthesis, which is itself part of Sulfur metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes glutathione from L-cysteine and L-glutamate, the pathway glutathione biosynthesis and in Sulfur metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Metal bindingi696Magnesium or manganese 1UniRule annotation1
    Metal bindingi717Magnesium or manganese 1UniRule annotation1
    Metal bindingi717Magnesium or manganese 2UniRule annotation1
    Metal bindingi719Magnesium or manganese 2UniRule annotation1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi516 – 574ATPUniRule annotationAdd BLAST59

    GO - Molecular functioni

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Glutathione biosynthesis

    Keywords - Ligandi

    ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi6.3.2.3. 5917.
    SABIO-RKQ8DXM9.
    UniPathwayiUPA00142; UER00209.
    UPA00142; UER00210.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione biosynthesis bifunctional protein GshABUniRule annotation
    Alternative name(s):
    Gamma-GCS-GSUniRule annotation
    Short name:
    GCS-GSUniRule annotation
    Including the following 2 domains:
    Glutamate--cysteine ligaseUniRule annotation (EC:6.3.2.2UniRule annotation)
    Alternative name(s):
    Gamma-ECSUniRule annotation
    Short name:
    GCSUniRule annotation
    Gamma-glutamylcysteine synthetaseUniRule annotation
    Glutathione synthetaseUniRule annotation (EC:6.3.2.3UniRule annotation)
    Alternative name(s):
    GSH synthetaseUniRule annotation
    Short name:
    GSUniRule annotation
    Short name:
    GSH-SUniRule annotation
    Short name:
    GSHaseUniRule annotation
    Glutathione synthaseUniRule annotation
    Gene namesi
    Name:gshABUniRule annotation
    Synonyms:gshFUniRule annotation
    Ordered Locus Names:SAG1821
    OrganismiStreptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R)
    Taxonomic identifieri208435 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
    Proteomesi
    • UP000000821 Componenti: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001925591 – 750Glutathione biosynthesis bifunctional protein GshABAdd BLAST750

    Interactioni

    Subunit structurei

    Monomer.Curated

    Structurei

    Secondary structure

    1750
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi7 – 9Combined sources3
    Beta strandi19 – 31Combined sources13
    Turni32 – 35Combined sources4
    Beta strandi44 – 46Combined sources3
    Turni49 – 51Combined sources3
    Beta strandi53 – 67Combined sources15
    Beta strandi71 – 73Combined sources3
    Helixi74 – 91Combined sources18
    Beta strandi96 – 98Combined sources3
    Beta strandi101 – 103Combined sources3
    Turni109 – 111Combined sources3
    Helixi120 – 133Combined sources14
    Helixi136 – 139Combined sources4
    Beta strandi143 – 149Combined sources7
    Helixi151 – 161Combined sources11
    Helixi166 – 191Combined sources26
    Beta strandi199 – 201Combined sources3
    Turni206 – 208Combined sources3
    Beta strandi212 – 214Combined sources3
    Beta strandi217 – 221Combined sources5
    Helixi234 – 243Combined sources10
    Turni246 – 248Combined sources3
    Helixi253 – 255Combined sources3
    Beta strandi259 – 264Combined sources6
    Turni268 – 274Combined sources7
    Beta strandi278 – 281Combined sources4
    Helixi296 – 311Combined sources16
    Helixi318 – 334Combined sources17
    Helixi347 – 361Combined sources15
    Helixi365 – 379Combined sources15
    Helixi381 – 383Combined sources3
    Helixi385 – 392Combined sources8
    Helixi399 – 413Combined sources15
    Helixi421 – 423Combined sources3
    Helixi428 – 440Combined sources13
    Beta strandi443 – 447Combined sources5
    Beta strandi449 – 451Combined sources3
    Beta strandi453 – 458Combined sources6
    Beta strandi461 – 466Combined sources6
    Turni467 – 469Combined sources3
    Helixi477 – 481Combined sources5
    Turni482 – 484Combined sources3
    Helixi486 – 494Combined sources9
    Turni507 – 510Combined sources4
    Helixi511 – 517Combined sources7
    Beta strandi518 – 521Combined sources4
    Beta strandi523 – 527Combined sources5
    Beta strandi532 – 535Combined sources4
    Beta strandi537 – 541Combined sources5
    Helixi545 – 558Combined sources14
    Beta strandi560 – 566Combined sources7
    Beta strandi570 – 578Combined sources9
    Beta strandi581 – 589Combined sources9
    Beta strandi592 – 594Combined sources3
    Helixi601 – 608Combined sources8
    Beta strandi614 – 618Combined sources5
    Beta strandi621 – 623Combined sources3
    Helixi629 – 637Combined sources9
    Beta strandi651 – 654Combined sources4
    Turni660 – 663Combined sources4
    Beta strandi665 – 668Combined sources4
    Turni670 – 672Combined sources3
    Helixi675 – 687Combined sources13
    Beta strandi694 – 700Combined sources7
    Beta strandi702 – 704Combined sources3
    Turni708 – 711Combined sources4
    Beta strandi714 – 721Combined sources8
    Helixi725 – 728Combined sources4
    Beta strandi731 – 733Combined sources3
    Helixi739 – 746Combined sources8

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3LN6X-ray2.95A1-750[»]
    ProteinModelPortaliQ8DXM9.
    SMRiQ8DXM9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini489 – 747ATP-graspUniRule annotationAdd BLAST259

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni1 – 333Glutamate--cysteine ligaseAdd BLAST333

    Sequence similaritiesi

    In the N-terminal section; belongs to the glutamate--cysteine ligase type 1 family. Type 2 subfamily.UniRule annotation
    Contains 1 ATP-grasp domain.UniRule annotation

    Phylogenomic databases

    HOGENOMiHOG000156471.
    KOiK01919.
    OMAiEANFNPM.

    Family and domain databases

    Gene3Di3.30.1490.20. 1 hit.
    3.30.470.20. 3 hits.
    HAMAPiMF_00782. Glut_biosynth. 1 hit.
    InterProiIPR011761. ATP-grasp.
    IPR013815. ATP_grasp_subdomain_1.
    IPR013816. ATP_grasp_subdomain_2.
    IPR007370. Glu_cys_ligase.
    IPR006335. Glut_biosynth.
    IPR020561. PRibGlycinamid_synth_ATP-grasp.
    [Graphical view]
    PfamiPF01071. GARS_A. 1 hit.
    PF04262. Glu_cys_ligase. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR01435. glu_cys_lig_rel. 1 hit.
    PROSITEiPS50975. ATP_GRASP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8DXM9-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MIIDRLLQRS HSHLPILQAT FGLERESLRI HQPTQRVAQT PHPKTLGSRN
    60 70 80 90 100
    YHPYIQTDYS EPQLELITPI AKDSQEAIRF LKAISDVAGR SINHDEYLWP
    110 120 130 140 150
    LSMPPKVREE DIQIAQLEDA FEYDYRKYLE KTYGKLIQSI SGIHYNLGLG
    160 170 180 190 200
    QELLTSLFEL SQADNAIDFQ NQLYMKLSQN FLRYRWLLTY LYGASPVAEE
    210 220 230 240 250
    DFLDQKLNNP VRSLRNSHLG YVNHKDIRIS YTSLKDYVND LENAVKSGQL
    260 270 280 290 300
    IAEKEFYSPV RLRGSKACRN YLEKGITYLE FRTFDLNPFS PIGITQETVD
    310 320 330 340 350
    TVHLFLLALL WIDSSSHIDQ DIKEANRLND LIALSHPLEK LPNQAPVSDL
    360 370 380 390 400
    VDAMQSVIQH FNLSPYYQDL LESVKRQIQS PELTVAGQLL EMIEGLSLET
    410 420 430 440 450
    FGQRQGQIYH DYAWEAPYAL KGYETMELST QLLLFDVIQK GVNFEVLDEQ
    460 470 480 490 500
    DQFLKLWHNS HIEYVKNGNM TSKDNYIVPL AMANKVVTKK ILDEKHFPTP
    510 520 530 540 550
    FGDEFTDRKE ALNYFSQIQD KPIVVKPKST NFGLGISIFK TSANLASYEK
    560 570 580 590 600
    AIDIAFTEDS AILVEEYIEG TEYRFFVLEG DCIAVLLRVA ANVVGDGIHT
    610 620 630 640 650
    ISQLVKLKNQ NPLRGYDHRS PLEVIELGEV EQLMLEQQGY TVNSIPPEGT
    660 670 680 690 700
    KIELRRNSNI STGGDSIDVT NTMDPTYKQL AAEMAEAMGA WVCGVDLIIP
    710 720 730 740 750
    NATQAYSKDK KNATCIELNF NPLMYMHTYC QEGPGQSITP RILAKLFPEL
    Length:750
    Mass (Da):85,603
    Last modified:March 1, 2003 - v1
    Checksum:i97829C2C5B44174A
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE009948 Genomic DNA. Translation: AAN00684.1.
    RefSeqiNP_688811.1. NC_004116.1.
    WP_000582678.1. NC_004116.1.

    Genome annotation databases

    EnsemblBacteriaiAAN00684; AAN00684; SAG1821.
    GeneIDi1014630.
    KEGGisag:SAG1821.
    PATRICi19630489. VBIStrAga72745_1829.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE009948 Genomic DNA. Translation: AAN00684.1.
    RefSeqiNP_688811.1. NC_004116.1.
    WP_000582678.1. NC_004116.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3LN6X-ray2.95A1-750[»]
    ProteinModelPortaliQ8DXM9.
    SMRiQ8DXM9.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAN00684; AAN00684; SAG1821.
    GeneIDi1014630.
    KEGGisag:SAG1821.
    PATRICi19630489. VBIStrAga72745_1829.

    Phylogenomic databases

    HOGENOMiHOG000156471.
    KOiK01919.
    OMAiEANFNPM.

    Enzyme and pathway databases

    UniPathwayiUPA00142; UER00209.
    UPA00142; UER00210.
    BRENDAi6.3.2.3. 5917.
    SABIO-RKQ8DXM9.

    Family and domain databases

    Gene3Di3.30.1490.20. 1 hit.
    3.30.470.20. 3 hits.
    HAMAPiMF_00782. Glut_biosynth. 1 hit.
    InterProiIPR011761. ATP-grasp.
    IPR013815. ATP_grasp_subdomain_1.
    IPR013816. ATP_grasp_subdomain_2.
    IPR007370. Glu_cys_ligase.
    IPR006335. Glut_biosynth.
    IPR020561. PRibGlycinamid_synth_ATP-grasp.
    [Graphical view]
    PfamiPF01071. GARS_A. 1 hit.
    PF04262. Glu_cys_ligase. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR01435. glu_cys_lig_rel. 1 hit.
    PROSITEiPS50975. ATP_GRASP. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiGSHAB_STRA5
    AccessioniPrimary (citable) accession number: Q8DXM9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 24, 2004
    Last sequence update: March 1, 2003
    Last modified: November 30, 2016
    This is version 90 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.